Investigating protein thiol chemistry associated with dehydroascorbate, homocysteine and glutathione using mass spectrometry.
Identifieur interne : 000056 ( Main/Exploration ); précédent : 000055; suivant : 000057Investigating protein thiol chemistry associated with dehydroascorbate, homocysteine and glutathione using mass spectrometry.
Auteurs : Grace Kouakou Ahuie [Canada] ; Hugo Gagnon [Canada] ; Paul E. Pace [Nouvelle-Zélande] ; Alexander V. Peskin [Nouvelle-Zélande] ; Richard J. Wagner [Canada] ; Stephen Naylor [États-Unis] ; Klaus Klarskov [Canada]Source :
- Rapid communications in mass spectrometry : RCM [ 1097-0231 ] ; 2020.
Abstract
RATIONALE
Oxidative stress is an imbalance between reactive free radical oxygen species and antioxidant defenses. Its consequences can lead to numerous pathologies. Regulating oxidative stress is the complex interplay between antioxidant recycling and thiol-containing regulatory proteins. Understanding these regulatory mechanisms is important for preventing onset of oxidative stress. The aim of this study was to investigae S-thiol protein chemistry associated with oxidized vitamin C (dehydroascorbate, DHA), homocysteine (HcySH) and glutathione (GSH) using mass spectrometry.
METHODS
Glutaredoxin-1 (Grx-1) was incubated with DHA, with and without GSH and HcySH. Disulfide formation was followed by electrospray ionization mass spectrometry (ESI-MS) of intact proteins and by LC/ESI-MS/MS of peptides from protein tryptic digestions. The mechanism of DHA-mediated S-thiolation was investigated using two synthetic peptides: AcFHACAAK and AcFHACE. Three proteins, i.e. human hemoglobin (HHb), recombinant peroxiredoxin 2 (Prdx2) and Grx-1, were S-homocysteinylated followed by S-transthiolyation with GSH and investigated by ESI-MS and ESI-MS/MS.
RESULTS
ESI-MS analysis reveals that DHA mediates disulfide formation and S-thiolation by HcySH as well as GSH of Grx-1. LC/ESI-MS/MS analysis allows identification of Grx-1 S-thiolated cysteine adducts. The mechanism by which DHA mediates S-thiolation of heptapeptide AcFHACAAK is shown to be via initial formation of a thiohemiketal adduct. In addition, ESI-MS of intact proteins shows that GSH can S-transthiolate S-homocysteinylated Grx-1_ HHb and Prdx2. The GS-S-protein adducts over time dominate the ESI-MS spectrum profile.
CONCLUSIONS
Mass spectrometry is a unique analytical technique for probing complex reaction mechanisms associated with oxidative stress. Using model proteins, ESI-MS reveals the mechanism of DHA-facilitated S-thiolation, which consists of thiohemiketal formation, disulfide formation or S-thiolation. Furthermore, protein S-thiolation by HcySH can be reversed by reversible GSH thiol exchange. The use of mass spectrometry with in vitro models of protein S-thiolation in oxidative stress may provide significant insight into possible mechanisms of action occurring in vivo.
DOI: 10.1002/rcm.8774
PubMed: 32119756
Affiliations:
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Pace</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Free Radical Research, University of Otago Christchurch, 2 Riccarton Avenue, Christchurch, 8140, New Zealand.</nlm:affiliation><country xml:lang="fr">Nouvelle-Zélande</country><wicri:regionArea>Centre for Free Radical Research, University of Otago Christchurch, 2 Riccarton Avenue, Christchurch, 8140</wicri:regionArea><wicri:noRegion>8140</wicri:noRegion></affiliation></author><author><name sortKey="Peskin, Alexander V" sort="Peskin, Alexander V" uniqKey="Peskin A" first="Alexander V" last="Peskin">Alexander V. 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Wagner</name><affiliation wicri:level="1"><nlm:affiliation>Département de Médecine Nucléaire et Radiobiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, 3001 Avenue Nord, Sherbrooke, Quebec, J1H 5N4, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Département de Médecine Nucléaire et Radiobiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, 3001 Avenue Nord, Sherbrooke, Quebec, J1H 5N4</wicri:regionArea><wicri:noRegion>J1H 5N4</wicri:noRegion></affiliation></author><author><name sortKey="Naylor, Stephen" sort="Naylor, Stephen" uniqKey="Naylor S" first="Stephen" last="Naylor">Stephen Naylor</name><affiliation wicri:level="1"><nlm:affiliation>ReNeuroGen LLC, 2160 San Fernando Drive, Elm Grove, WI, 53122, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>ReNeuroGen LLC, 2160 San Fernando Drive, Elm Grove, WI, 53122</wicri:regionArea><wicri:noRegion>53122</wicri:noRegion></affiliation></author><author><name sortKey="Klarskov, Klaus" sort="Klarskov, Klaus" uniqKey="Klarskov K" first="Klaus" last="Klarskov">Klaus Klarskov</name><affiliation wicri:level="1"><nlm:affiliation>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, 3001 Avenue Nord, Sherbrooke, Quebec, J1H 5N4, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, 3001 Avenue Nord, Sherbrooke, Quebec, J1H 5N4</wicri:regionArea><wicri:noRegion>J1H 5N4</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:32119756</idno><idno type="pmid">32119756</idno><idno type="doi">10.1002/rcm.8774</idno><idno type="wicri:Area/Main/Corpus">000077</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000077</idno><idno type="wicri:Area/Main/Curation">000077</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000077</idno><idno type="wicri:Area/Main/Exploration">000077</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Investigating protein thiol chemistry associated with dehydroascorbate, homocysteine and glutathione using mass spectrometry.</title><author><name sortKey="Ahuie, Grace Kouakou" sort="Ahuie, Grace Kouakou" uniqKey="Ahuie G" first="Grace Kouakou" last="Ahuie">Grace Kouakou Ahuie</name><affiliation wicri:level="1"><nlm:affiliation>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, 3001 Avenue Nord, Sherbrooke, Quebec, J1H 5N4, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, 3001 Avenue Nord, Sherbrooke, Quebec, J1H 5N4</wicri:regionArea><wicri:noRegion>J1H 5N4</wicri:noRegion></affiliation></author><author><name sortKey="Gagnon, Hugo" sort="Gagnon, Hugo" uniqKey="Gagnon H" first="Hugo" last="Gagnon">Hugo Gagnon</name><affiliation wicri:level="1"><nlm:affiliation>PhenoSwitch Bioscience, 975 Rue Léon-Trépanier, Sherbrooke, Quebec, J1G 5J6, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>PhenoSwitch Bioscience, 975 Rue Léon-Trépanier, Sherbrooke, Quebec, J1G 5J6</wicri:regionArea><wicri:noRegion>J1G 5J6</wicri:noRegion></affiliation></author><author><name sortKey="Pace, Paul E" sort="Pace, Paul E" uniqKey="Pace P" first="Paul E" last="Pace">Paul E. Pace</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Free Radical Research, University of Otago Christchurch, 2 Riccarton Avenue, Christchurch, 8140, New Zealand.</nlm:affiliation><country xml:lang="fr">Nouvelle-Zélande</country><wicri:regionArea>Centre for Free Radical Research, University of Otago Christchurch, 2 Riccarton Avenue, Christchurch, 8140</wicri:regionArea><wicri:noRegion>8140</wicri:noRegion></affiliation></author><author><name sortKey="Peskin, Alexander V" sort="Peskin, Alexander V" uniqKey="Peskin A" first="Alexander V" last="Peskin">Alexander V. Peskin</name><affiliation wicri:level="1"><nlm:affiliation>Centre for Free Radical Research, University of Otago Christchurch, 2 Riccarton Avenue, Christchurch, 8140, New Zealand.</nlm:affiliation><country xml:lang="fr">Nouvelle-Zélande</country><wicri:regionArea>Centre for Free Radical Research, University of Otago Christchurch, 2 Riccarton Avenue, Christchurch, 8140</wicri:regionArea><wicri:noRegion>8140</wicri:noRegion></affiliation></author><author><name sortKey="Wagner, Richard J" sort="Wagner, Richard J" uniqKey="Wagner R" first="Richard J" last="Wagner">Richard J. Wagner</name><affiliation wicri:level="1"><nlm:affiliation>Département de Médecine Nucléaire et Radiobiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, 3001 Avenue Nord, Sherbrooke, Quebec, J1H 5N4, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Département de Médecine Nucléaire et Radiobiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, 3001 Avenue Nord, Sherbrooke, Quebec, J1H 5N4</wicri:regionArea><wicri:noRegion>J1H 5N4</wicri:noRegion></affiliation></author><author><name sortKey="Naylor, Stephen" sort="Naylor, Stephen" uniqKey="Naylor S" first="Stephen" last="Naylor">Stephen Naylor</name><affiliation wicri:level="1"><nlm:affiliation>ReNeuroGen LLC, 2160 San Fernando Drive, Elm Grove, WI, 53122, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>ReNeuroGen LLC, 2160 San Fernando Drive, Elm Grove, WI, 53122</wicri:regionArea><wicri:noRegion>53122</wicri:noRegion></affiliation></author><author><name sortKey="Klarskov, Klaus" sort="Klarskov, Klaus" uniqKey="Klarskov K" first="Klaus" last="Klarskov">Klaus Klarskov</name><affiliation wicri:level="1"><nlm:affiliation>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, 3001 Avenue Nord, Sherbrooke, Quebec, J1H 5N4, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, 3001 Avenue Nord, Sherbrooke, Quebec, J1H 5N4</wicri:regionArea><wicri:noRegion>J1H 5N4</wicri:noRegion></affiliation></author></analytic><series><title level="j">Rapid communications in mass spectrometry : RCM</title><idno type="eISSN">1097-0231</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>RATIONALE</b></p><p>Oxidative stress is an imbalance between reactive free radical oxygen species and antioxidant defenses. Its consequences can lead to numerous pathologies. Regulating oxidative stress is the complex interplay between antioxidant recycling and thiol-containing regulatory proteins. Understanding these regulatory mechanisms is important for preventing onset of oxidative stress. The aim of this study was to investigae S-thiol protein chemistry associated with oxidized vitamin C (dehydroascorbate, DHA), homocysteine (HcySH) and glutathione (GSH) using mass spectrometry.</p></div><div type="abstract" xml:lang="en"><p><b>METHODS</b></p><p>Glutaredoxin-1 (Grx-1) was incubated with DHA, with and without GSH and HcySH. Disulfide formation was followed by electrospray ionization mass spectrometry (ESI-MS) of intact proteins and by LC/ESI-MS/MS of peptides from protein tryptic digestions. The mechanism of DHA-mediated S-thiolation was investigated using two synthetic peptides: AcFHACAAK and AcFHACE. Three proteins, i.e. human hemoglobin (HHb), recombinant peroxiredoxin 2 (Prdx2) and Grx-1, were S-homocysteinylated followed by S-transthiolyation with GSH and investigated by ESI-MS and ESI-MS/MS.</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>ESI-MS analysis reveals that DHA mediates disulfide formation and S-thiolation by HcySH as well as GSH of Grx-1. LC/ESI-MS/MS analysis allows identification of Grx-1 S-thiolated cysteine adducts. The mechanism by which DHA mediates S-thiolation of heptapeptide AcFHACAAK is shown to be via initial formation of a thiohemiketal adduct. In addition, ESI-MS of intact proteins shows that GSH can S-transthiolate S-homocysteinylated Grx-1_ HHb and Prdx2. The GS-S-protein adducts over time dominate the ESI-MS spectrum profile.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSIONS</b></p><p>Mass spectrometry is a unique analytical technique for probing complex reaction mechanisms associated with oxidative stress. Using model proteins, ESI-MS reveals the mechanism of DHA-facilitated S-thiolation, which consists of thiohemiketal formation, disulfide formation or S-thiolation. Furthermore, protein S-thiolation by HcySH can be reversed by reversible GSH thiol exchange. The use of mass spectrometry with in vitro models of protein S-thiolation in oxidative stress may provide significant insight into possible mechanisms of action occurring in vivo.</p></div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">32119756</PMID><DateRevised><Year>2020</Year><Month>05</Month><Day>22</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1097-0231</ISSN><JournalIssue CitedMedium="Internet"><Volume>34</Volume><Issue>11</Issue><PubDate><Year>2020</Year><Month>Jun</Month><Day>15</Day></PubDate></JournalIssue><Title>Rapid communications in mass spectrometry : RCM</Title><ISOAbbreviation>Rapid Commun Mass Spectrom</ISOAbbreviation></Journal><ArticleTitle>Investigating protein thiol chemistry associated with dehydroascorbate, homocysteine and glutathione using mass spectrometry.</ArticleTitle><Pagination><MedlinePgn>e8774</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/rcm.8774</ELocationID><Abstract><AbstractText Label="RATIONALE" NlmCategory="BACKGROUND">Oxidative stress is an imbalance between reactive free radical oxygen species and antioxidant defenses. Its consequences can lead to numerous pathologies. Regulating oxidative stress is the complex interplay between antioxidant recycling and thiol-containing regulatory proteins. Understanding these regulatory mechanisms is important for preventing onset of oxidative stress. The aim of this study was to investigae S-thiol protein chemistry associated with oxidized vitamin C (dehydroascorbate, DHA), homocysteine (HcySH) and glutathione (GSH) using mass spectrometry.</AbstractText><AbstractText Label="METHODS" NlmCategory="METHODS">Glutaredoxin-1 (Grx-1) was incubated with DHA, with and without GSH and HcySH. Disulfide formation was followed by electrospray ionization mass spectrometry (ESI-MS) of intact proteins and by LC/ESI-MS/MS of peptides from protein tryptic digestions. The mechanism of DHA-mediated S-thiolation was investigated using two synthetic peptides: AcFHACAAK and AcFHACE. Three proteins, i.e. human hemoglobin (HHb), recombinant peroxiredoxin 2 (Prdx2) and Grx-1, were S-homocysteinylated followed by S-transthiolyation with GSH and investigated by ESI-MS and ESI-MS/MS.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">ESI-MS analysis reveals that DHA mediates disulfide formation and S-thiolation by HcySH as well as GSH of Grx-1. LC/ESI-MS/MS analysis allows identification of Grx-1 S-thiolated cysteine adducts. The mechanism by which DHA mediates S-thiolation of heptapeptide AcFHACAAK is shown to be via initial formation of a thiohemiketal adduct. In addition, ESI-MS of intact proteins shows that GSH can S-transthiolate S-homocysteinylated Grx-1_ HHb and Prdx2. The GS-S-protein adducts over time dominate the ESI-MS spectrum profile.</AbstractText><AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">Mass spectrometry is a unique analytical technique for probing complex reaction mechanisms associated with oxidative stress. Using model proteins, ESI-MS reveals the mechanism of DHA-facilitated S-thiolation, which consists of thiohemiketal formation, disulfide formation or S-thiolation. Furthermore, protein S-thiolation by HcySH can be reversed by reversible GSH thiol exchange. The use of mass spectrometry with in vitro models of protein S-thiolation in oxidative stress may provide significant insight into possible mechanisms of action occurring in vivo.</AbstractText><CopyrightInformation>© 2020 John Wiley & Sons, Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ahuie</LastName><ForeName>Grace Kouakou</ForeName><Initials>GK</Initials><AffiliationInfo><Affiliation>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, 3001 Avenue Nord, Sherbrooke, Quebec, J1H 5N4, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gagnon</LastName><ForeName>Hugo</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>PhenoSwitch Bioscience, 975 Rue Léon-Trépanier, Sherbrooke, Quebec, J1G 5J6, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pace</LastName><ForeName>Paul E</ForeName><Initials>PE</Initials><AffiliationInfo><Affiliation>Centre for Free Radical Research, University of Otago Christchurch, 2 Riccarton Avenue, Christchurch, 8140, New Zealand.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Peskin</LastName><ForeName>Alexander V</ForeName><Initials>AV</Initials><AffiliationInfo><Affiliation>Centre for Free Radical Research, University of Otago Christchurch, 2 Riccarton Avenue, Christchurch, 8140, New Zealand.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wagner</LastName><ForeName>Richard J</ForeName><Initials>RJ</Initials><AffiliationInfo><Affiliation>Département de Médecine Nucléaire et Radiobiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, 3001 Avenue Nord, Sherbrooke, Quebec, J1H 5N4, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Naylor</LastName><ForeName>Stephen</ForeName><Initials>S</Initials><Identifier Source="ORCID">https://orcid.org/0000-0001-7619-6044</Identifier><AffiliationInfo><Affiliation>ReNeuroGen LLC, 2160 San Fernando Drive, Elm Grove, WI, 53122, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Klarskov</LastName><ForeName>Klaus</ForeName><Initials>K</Initials><Identifier Source="ORCID">https://orcid.org/0000-0001-7574-7537</Identifier><AffiliationInfo><Affiliation>Département de Pharmacologie et Physiologie, Faculté de Médecine et des Sciences de la Santé, Université de Sherbrooke, 3001 Avenue Nord, Sherbrooke, Quebec, J1H 5N4, Canada.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Rapid Commun Mass Spectrom</MedlineTA><NlmUniqueID>8802365</NlmUniqueID><ISSNLinking>0951-4198</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>07</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>01</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>02</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>3</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>3</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>3</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32119756</ArticleId><ArticleId IdType="doi">10.1002/rcm.8774</ArticleId></ArticleIdList><ReferenceList><Title>REFERENCES</Title><Reference><Citation>Govindpani K, McNamara LG, Smith NR, et al. 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Pace</name></noRegion><name sortKey="Peskin, Alexander V" sort="Peskin, Alexander V" uniqKey="Peskin A" first="Alexander V" last="Peskin">Alexander V. Peskin</name></country><country name="États-Unis"><noRegion><name sortKey="Naylor, Stephen" sort="Naylor, Stephen" uniqKey="Naylor S" first="Stephen" last="Naylor">Stephen Naylor</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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